Pure and Applied Chemistry

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• Hong Zhenmin, Ahmed Zeeshan, Asher Sanford A.: Circular Dichroism and Ultraviolet Resonance Raman Indicate Little Arg-Glu Side Chain α-Helix Peptide Stabilization. J Phys Chem B 2011, 115, 4234. <http://dx.doi.org/10.1021/jp112238q>
• Anteunis Marc J. O.: The cyclic dipeptides. Proper model compounds in peptide research. Bull Soc Chim Belges 2010, 87, 627. <http://dx.doi.org/10.1002/bscb.19780870808>
• Skwierawska Agnieszka, Żmudzińska Wioletta, Ołdziej Stanisław, Liwo Adam, Scheraga Harold A.: Mechanism of formation of the C-terminal β-hairpin of the B3 domain of the immunoglobulin binding protein G from Streptococcus. II. Interplay of local backbone conformational dynamics and long-range hydrophobic interactions in hairpin formation. Proteins 2009, 76, 637. <http://dx.doi.org/10.1002/prot.22377>
• Bandekar Jagdeesh: A SIMPLE MODEL FOR PROTEIN THERMAL DENATURATION*. International journal of peptide & protein research 2009, 11, 191. <http://dx.doi.org/10.1111/j.1399-3011.1978.tb02839.x>
• GO NOBUHIRO, TAKETOMI HIROSHI: STUDIES ON PROTEIN FOLDING, UNFOLDING AND FLUCTUATIONS BY COMPUTER SIMULATION III. Effect of Short-Range Interactions. International journal of peptide & protein research 2009, 13, 235. <http://dx.doi.org/10.1111/j.1399-3011.1979.tb01875.x>
• BENEDETTI ETTORE, MORELLI GIANCARLO, NÉMETHY GEORGE, SCHERAGA HAROLD A.: Statistical and energetic analysis of side-chain conformations in oligopeptides. International journal of peptide & protein research 2009, 22, 1. <http://dx.doi.org/10.1111/j.1399-3011.1983.tb02062.x>
• ISHII HIROSHI, INOUE YOSHIO, CHÛJÔ RIICHIRÔ: Conformational study of glycopeptides : Asn-containing peptides and their glycosylated derivatives. Int J Peptide Protein Res 2009, 24, 421. <http://dx.doi.org/10.1111/j.1399-3011.1984.tb03140.x>
• Vila Jorge A., Baldoni Héctor A., Scheraga Harold A.: Position dependence of the 13C chemical shifts of α-helical model peptides. Fingerprint of the 20 naturally occurring amino acids. Protein Sci 2008, 13, 2939. <http://dx.doi.org/10.1110/ps.04930804>
• Lin Milo M., Shorokhov Dmitry, Zewail Ahmed H.: Helix-to-coil transitions in proteins: Helicity resonance in ultrafast electron diffraction. chem phys letts 2006, 420, 1. <http://dx.doi.org/10.1016/j.cplett.2005.11.088>
• Prasad Onkar, Sinha Leena, Gupta G.P., Agnihotri R.C., Misra N., Lal J.N.: Theoretical study of temperature induced phase transitions in poly(β-benzyl-l-aspartate) and it's copolymer. Polymer 2005, 46, 7450. <http://dx.doi.org/10.1016/j.polymer.2005.06.020>
• Prasad Onkar, Sinha Leena, Misra Neeraj, Gupta Govind P., Agnihotri Ramesh C.: Pressure induced order–disorder transition in a diblock copolymer. Polymer 2005, 46, 11876. <http://dx.doi.org/10.1016/j.polymer.2005.10.035>
• Vila Jorge A., Ripoll Daniel R., Scheraga Harold A.: Influence of lysine content and PH on the stability of alanine-based copolypeptides. Biopolymers (Biospectroscopy) 2001, 58, 235. <http://dx.doi.org/10.1002/1097-0282(200103)58:3<235::AID-BIP1001>3.0.CO;2-T>
• Borg Jesper, Jensen Mogens, Sneppen Kim, Tiana Guido: Hydrogen Bonds in Polymer Folding. Phys Rev Letters 2001, 86, 1031. <http://dx.doi.org/10.1103/PhysRevLett.86.1031>
• Tropsha Alexander, Hermans Jan, O'Connell Thomas M., Wang Lu: The “random-coil” state of proteins: Comparison of database statistics and molecular simulations. Proteins 1999, 36, 407. <http://dx.doi.org/10.1002/(SICI)1097-0134(19990901)36:4<407::AID-PROT4>3.0.CO;2-1>
• Lindemann Almut, Kinzel Volker, Rösch Paul, Reed Jennifer: Structure of the LAV6 peptide: A nucleation site for the correct receptor-induced refolding of the CD4-binding domain of HIV1 gp 120. Proteins 1997, 29, 203. <http://dx.doi.org/10.1002/(SICI)1097-0134(199710)29:2<203::AID-PROT8>3.0.CO;2-D>
• Singh Tej P., Kaur Punit: Conformation and design of peptides with α,β-dehydro-amino acid residues. Prog Biophys Molec Biol 1996, 66, 141. <http://dx.doi.org/10.1016/S0079-6107(97)85628-3>
• Silaghi-Dumitrescu Ioan, Lara-Ochoa Francisco, Haiduc Ionel, Stinchcomb David M., Pranata Julianto, Klein Christian Th., Mayer Bernd, K��hler Gottfried, Wolschann Peter: A12B12 (A = B,Al; B = N,P) fullerene-like cages and their hydrogenated forms stabilized by exohedral bonds. An AM1 molecular orbital study. Journal of Molecular Structure: THEOCHEM 1996, 370, 17. <http://dx.doi.org/10.1016/S0166-1280(96)04745-8>
• Timoshenko E., Kuznetsov Yu., Dawson K.: Kinetics of a Gaussian random copolymer as a prototype for protein folding. Phys Rev E 1996, 54, 4071. <http://dx.doi.org/10.1103/PhysRevE.54.4071>
• Parthasarathy R., Chaturvedi Sanjeev, Go Kuantee: Design of α-helical peptides: Their role in protein folding and molecular biology. Prog Biophys Molec Biol 1995, 64, 1. <http://dx.doi.org/10.1016/0079-6107(95)00009-7>
• Ohshima Kunihiro, Okabayashi Hirofumi, Yoshida Tadayoshi: Folded structure induction effect of an L-leucine residue on the conformations of L-leucylglycine oligomers: vibrational spectroscopic evidence. Vib Spect 1995, 8, 401. <http://dx.doi.org/10.1016/0924-2031(94)00056-M>
• Timoshenko E. G., Kuznetsov Yu. A., Dawson K. A.: Kinetics at the collapse transition Gaussian self-consistent approach. J Chem Phys 1995, 102, 1816. <http://dx.doi.org/10.1063/1.468709>
• Hao Ming-Hong, Scheraga Harold A.: Statistical thermodynamics of protein folding: Comparison of a mean-field theory with Monte Carlo simulations. J Chem Phys 1995, 102, 1334. <http://dx.doi.org/10.1063/1.468920>
• Kuznetsov Yu. A., Timoshenko E. G., Dawson K. A.: Kinetics at the collapse transition of homopolymers and random copolymers. J Chem Phys 1995, 103, 4807. <http://dx.doi.org/10.1063/1.470615>
• Dawson K. A., Timoshenko E. G., Kiernan P.: Theoretical and experimental approaches to kinetics at the collapse transition of a homopolymer. Nuovo Cimento 1994, 16, 675. <http://dx.doi.org/10.1007/BF02456712>
• Piela Lucjan, Olszewski Krzysztof A., Pillardy Jarostaw: On the stability of conformers. Journal of Molecular Structure: THEOCHEM 1994, 308, 229. <http://dx.doi.org/10.1016/0166-1280(94)80105-3>
• Daggett Valerie, Levitt Michael: Molecular dynamics simulations of helix denaturation. Journal of Molecular Biology 1992, 223, 1121. <http://dx.doi.org/10.1016/0022-2836(92)90264-K>
• Daggett Valerie, Kollman Peter A., Kuntz Irwin D.: A molecular dynamics simulation of polyalanine: An analysis of equilibrium motions and helix-coil transitions. Biopolymers (Biospectroscopy) 1991, 31, 1115. <http://dx.doi.org/10.1002/bip.360310911>
• Wójcik J., Altmann K.-H., Scheraga H. A.: Helix-coil stability constants for the naturally occurring amino acids in water. XXIV. Half-cystine parameters from random poly(hydroxybutylglutamine-CO-S-methylthio-L-cysteine). Biopolymers (Biospectroscopy) 1990, 30, 121. <http://dx.doi.org/10.1002/bip.360300113>
• Roterman I. K., Lambert M. H., Gibson K. D., Scheraga H. A.: A Comparison of the CHARMM, AMBER and ECEPP Potentials for Peptides. II. φ-ψ Maps for N-Acetyl Alanine N′-Methyl Amide: Comparisons, Contrasts and Simple Experimental Tests. Journal of Biomolecular Structure & Dynamics 1989, 7, 421. <http://dx.doi.org/10.1080/07391102.1989.10508503>
• Vásquez Maximiliano, Scheraga Harold A.: Calculation of Protein Conformation by the Build-up Procedure. Application to Bovine Pancreatic Trypsin Inhibitor Using Limited Simulated Nuclear Magnetic Resonance Data. J Biomol Struct Dyn 1988, 5, 705. <http://dx.doi.org/10.1080/07391102.1988.10506425>
• Vásquez Maximiliano, Scheraga Harold A.: Variable-Target-Function and Build-up Procedures for the Calculation of Protein Conformation. Application to Bovine Pancreatic Trypsin Inhibitor Using Limited Simulated Nuclear Magnetic Resonance Data. J Biomol Struct Dyn 1988, 5, 757. <http://dx.doi.org/10.1080/07391102.1988.10506426>
• Piela Lucjan, Nemethy George, Scheraga Harold A.: Conformational constraints of amino acid side chains in α-helices. Biopolymers (Biospectroscopy) 1987, 26, 1273. <http://dx.doi.org/10.1002/bip.360260805>
• Mutter Manfred: Die Konstruktion von neuen Proteinen und Enzymen - eine Zukunftsperspektive?. Angew Chem 1985, 97, 639. <http://dx.doi.org/10.1002/ange.19850970805>
• Mutter Manfred: The Construction of New Proteins and Enzymes-a Prospect for the Future?. Angew Chem Int Ed Engl 1985, 24, 639. <http://dx.doi.org/10.1002/anie.198506391>
• Bode Karsten, Goodman Murray, Mutter Manfred: Conformational Studies on Potential β-Turn-Forming Model Peptides. HCA 1985, 68, 705. <http://dx.doi.org/10.1002/hlca.19850680320>
• Scheraga Harold A.: Protein structure and function, from a colloidal to a molecular view. Carlsberg Res Commun 1984, 49, 1. <http://dx.doi.org/10.1007/BF02913964>
• Scheraga Harold A.: Recent progress in the theoretical treatment of protein folding. Biopolymers (Biospectroscopy) 1983, 22, 1. <http://dx.doi.org/10.1002/bip.360220104>
• Rao Ch. Pulla, Balaram P., Rao C. N. R.: Infrared spectroscopic study of C7 intramolecular hydrogen bonds in peptides. Biopolymers (Biospectroscopy) 1983, 22, 2091. <http://dx.doi.org/10.1002/bip.360220908>
• Wako Hiroshi, Saitô Nobuhiko, Scheraga Harold A.: Statistical mechanical treatment of α-helices and extended structures in proteins with inclusion of short- and medium-range interactions. J Protein Chem 1983, 2, 221. <http://dx.doi.org/10.1007/BF01025356>
• Anderson J. S., Scheraga H. A.: Effect of short- and long-range interactions on protein folding. J Protein Chem 1982, 1, 281. <http://dx.doi.org/10.1007/BF01039553>
• Simon I.: Possible mechanism for the dynamic stabilization of protein structure. J Theor Biol 1981, 90, 487. <http://dx.doi.org/10.1016/0022-5193(81)90301-5>
• Zientara Gary P., Nagy Janice A., Freed Jack H.: Diffusion-controlled kinetics of protein domain coalescence: Effects of orientation, interdomain forces and hydration. J Chem Phys 1980, 73, 5092. <http://dx.doi.org/10.1063/1.439987>
• Scheraga Harold A.: Phase transitions in synthetic polymers of amino acids, and their relation to protein folding. GFER 1980, 30, 157. <http://dx.doi.org/10.1080/00150198008209507>
• Toniolo Claudio, Benedetti Ettore: Intramolecularly Hydrogen-Bonded Peptide Conformation. Crit Rev Biochem Mol Biol 1980, 9, 1. <http://dx.doi.org/10.3109/10409238009105471>
• Hodes Zachary I., Némethy George, Scheraga Harold A.: Model for the conformational analysis of hydrated peptides. Effect of hydration on the conformational stability of the terminally blocked residues of the 20 naturally occurring amino acids. Biopolymers (Biospectroscopy) 1979, 18, 1565. <http://dx.doi.org/10.1002/bip.1979.360180702>
• Hodes Zachary I., Némethy George, Scheraga Harold A.: Influence of hydration on the conformational stability and formation of bends in terminally blocked dipeptides. Biopolymers (Biospectroscopy) 1979, 18, 1611. <http://dx.doi.org/10.1002/bip.1979.360180703>
• Maxfield F. R., Leach S. J., Stimson E. R., Powers S. P., Scheraga H. A.: Infrared spectra of theN-acetyl-N′-methylamides of glycine,L-alanine, andL-leucine in dilute solutions of chloroform and carbon tetrachloride. Biopolymers (Biospectroscopy) 1979, 18, 2507. <http://dx.doi.org/10.1002/bip.1979.360181010>
• Creighton Thomas E.: Experimental studies of protein folding and unfolding. Prog Biophys Molec Biol 1979, 33, 231. <http://dx.doi.org/10.1016/0079-6107(79)90030-0>
• Zimmerman S. Scott, Scheraga Harold A.: Influence of local interactions on protein structure. II. Conformational energy studies ofN-acetyl-N′-methylamides of Ala-X and X-Ala dipeptides. Biopolymers (Biospectroscopy) 1978, 17, 1849. <http://dx.doi.org/10.1002/bip.1978.360170804>
• Creighton T.E., Dyckes D.F., Sheppard R.C.: Refolding of bovine pancreatic trypsin inhibitor modified at methionine-52. Journal of Molecular Biology 1978, 119, 507. <http://dx.doi.org/10.1016/0022-2836(78)90199-7>
• Zimmerman S. Scott, Scheraga Harold A.: Influence of local interactions on protein structure. I. Conformational energy studies ofN-acetyl-N′-methylamides of pro-X and X-pro dipeptides. Biopolymers (Biospectroscopy) 1977, 16, 811. <http://dx.doi.org/10.1002/bip.1977.360160408>
• Matheson R. R., Nemenoff R. A., Cardinaux F., Scheraga H. A.: Helix-coil stability constants for the naturally occurring amino acids in water. XII. Asparagine parameters from random poly(hydroxybutylglutamine-co-L-asparagine). Biopolymers (Biospectroscopy) 1977, 16, 1567. <http://dx.doi.org/10.1002/bip.1977.360160715>
• Hill D. J. T., Cardinaux F., Scheraga H. A.: Helix-coil stability constants for the naturally occuring amino acids in water. XIV. Methionine parameters from random poly(hydroxypropylglutamine,L-Methionine). Biopolymers (Biospectroscopy) 1977, 16, 2447. <http://dx.doi.org/10.1002/bip.1977.360161109>
• Vellaccio F., Punzar R.V., Kemp D.S.: The reaction of dialkylmalonyl dichlorides with 1,3-diaminopropanes a new route to macrocyclic polyamides and polyamines. Tetrahetron Lett 1977, 18, 547. <http://dx.doi.org/10.1016/S0040-4039(01)92690-5>
• Némethy George, Scheraga Harold A.: Protein folding. Quart Rev Biophys 1977, 10, 239. <http://dx.doi.org/10.1017/S0033583500002936>
• Kopple Kenneth D., Go Anita: Studies of peptide conformation: Backbone folding of tetrapeptide derivatives in methanol and water. Biopolymers (Biospectroscopy) 1976, 15, 1701. <http://dx.doi.org/10.1002/bip.1976.360150908>
• Fu Yi-Chang, Van Wart Harold E., Scheraga Harold A.: Calorimetric measurement of enthalpy change in the isothermal helix-coil transition of poly(L-ornithine) in aqueous solution. Biopolymers (Biospectroscopy) 1976, 15, 1795. <http://dx.doi.org/10.1002/bip.1976.360150913>
• Burgess A.W., Scheraga H.A.: A hypothesis for the pathway of the thermally-induced unfolding of bovine pancreatic ribonuclease. J Theor Biol 1975, 53, 403. <http://dx.doi.org/10.1016/S0022-5193(75)80012-9>